SNARE proteins are a group of membrane-associated proteins involved in exocytosis, secretion and membrane trafficking events in eukaryotic cells. Research on SNARE protein biology has become a more attractive field in...SNARE proteins are a group of membrane-associated proteins involved in exocytosis, secretion and membrane trafficking events in eukaryotic cells. Research on SNARE protein biology has become a more attractive field in recent years, which is applied to marine biology specifically to the fish Tilapia （Oreochromis niloticus）. Plasma membrane fractions of different tissues of Tilapia, including brain, liver-pancreas, intestine, skin and muscle, were extracted, and immuno-decorated with isoform-specific antibodies to the SNARE families and associated proteins. The presence of Syntaxins - 1 A, 2 and 3, SNAP - 23 and SNAP - 25, VAMP - 2, Munc - 18 - 1 and Munc - 13 in the brain was identified, which were differentially distributed in the other organ tissues of the fish Tilapia. The distinct distribution of SNARE and associated proteins will serve as the basis for further investigation into their special secretory function in these tissues of the fish.展开更多
The role of SNARE [soluble NSF (N-ethylmaleimide-sensitive factor) accessory protein receptor] protein in cellular trafficking, membrane fusion and vesicle release in synaptic nerve terminals is described. The purpose...The role of SNARE [soluble NSF (N-ethylmaleimide-sensitive factor) accessory protein receptor] protein in cellular trafficking, membrane fusion and vesicle release in synaptic nerve terminals is described. The purpose of this review is to highlight the role of SNAREs in vital inflammatory conditions in maturing dendritic cells in order to retain the capacity to present new antigens together with altered cytokine secretory functions. This role of SNAREs can be used as novel targets for therapy in inflammatory diseases. The essential mechanism of SNAREs proteins for regulation of tumour formation through multiple signals and transportation pathways is also discussed. Finally, this review summarizes the current knowledge of SNARE proteins in regulating endocytosis in cancer cells and the possible therapeutic applications related to the pathogenesis of tumor formation.展开更多
Through complex mechanisms that guide axons to the appropriate routes towards their targets, axonal growth and guidance lead to neuronal system formation. These mechanisms establish the synaptic circuitry necessary fo...Through complex mechanisms that guide axons to the appropriate routes towards their targets, axonal growth and guidance lead to neuronal system formation. These mechanisms establish the synaptic circuitry necessary for the optimal performance of the nervous system in all organisms. Damage to these networks can be repaired by neuroregenerative processes which in turn can re-establish synapses between injured axons and postsynaptic terminals. Both axonal growth and guidance and the neuroregenerative response rely on correct axonal growth and growth cone responses to guidance cues as well as correct synapses with appropriate targets. With this in mind, parallels can be drawn between axonal regeneration and processes occurring during embryonic nervous system development. However, when studying parallels between axonal development and regeneration many questions still arise; mainly, how do axons grow and synapse with their targets and how do they repair their membranes, grow and orchestrate regenerative responses after injury. Major players in the cellular and molecular processes that lead to growth cone development and movement during embryonic development are the Soluble N-ethylamaleimide Sensitive Factor （NSF） Attachment Protein Receptor （SNARE） proteins, which have been shown to be involved in axonal growth and guidance. Their involvement in axonal growth, guidance and neuroregeneration is of foremost importance, due to their roles in vesicle and membrane trafficking events. Here, we review the recent literature on the involvement of SNARE proteins in axonal growth and guidance during embryonic development and neuroregeneration.展开更多
目的分离体外培养的结核分枝杆菌分泌的膜囊泡，检测其形态和粒径分布，初步探索结核分枝杆菌膜囊泡对巨噬细胞中细胞因子释放的作用。方法采用结核分枝杆菌实验室标准菌株H37Rv，通过7H9培养基复苏、扩大培养标准株H37Rv至对数生长期...目的分离体外培养的结核分枝杆菌分泌的膜囊泡，检测其形态和粒径分布，初步探索结核分枝杆菌膜囊泡对巨噬细胞中细胞因子释放的作用。方法采用结核分枝杆菌实验室标准菌株H37Rv，通过7H9培养基复苏、扩大培养标准株H37Rv至对数生长期，菌体全部接种于苏通培养基中继续培养3周，离心取上清，超滤浓缩结合超速离心分离提取结核分枝杆菌H37Rv膜囊泡，通过透射电镜观察膜囊泡的大小、形态，采用纳米颗粒跟踪仪分析膜囊泡的粒径及分布。同时，设置不处理对照组、H37Rv感染组[按照感染复数（multiplicity of infection，MOI）=20：1]和H37Rv膜囊泡处理组（按照膜囊泡：细胞=100：1）处理佛波酯（50ng／ml）诱导贴壁的单核巨噬细胞（THP-1）4h，更换新鲜培养基后0h、4h、8h、24h收集细胞培养上清，采用Milliplex多细胞因子检测试剂盒检测细胞因子的释放情况，通过曼-惠特尼U（Mann-WhitneyU）检验对各时间点H37Rv膜囊泡处理组和不处理对照组之间肿瘤坏死因子α（TNF-α）、白细胞介素6（IL-6）、白细胞介素1β（IL-1β）、白细胞介素10（IL-10）释放量进行比较，以P〈0．05为差异有统计学意义。结果按照调整后的提取方法得到的提取物中可检测到H37Rv分泌的膜囊泡，平均粒径为137nm，主要分布在30～510nm之间，〈250nm的膜囊泡数量占总量的96．88％。4h、8h和24h的TNF-α、ID6和IL-1β释放量与不处理对照组[分别为348．19（333．99，360．47）pg／ml、412．38（406．67，418．79）pg／ml、324．44（316．11，331．14）pg／ml；3．01（2．81，3．02）pg／ml、5．40（5．26，5．83）pg／ml、13．22（11．80，13．77）pg／ml；118．92（113．97，122．47）pg／ml、132．33（125．87，137．62）pg／ml、169．31（167．75，172．49）pg／ml]相比，H37Rv膜囊泡处理组[分别为507．33（501．80，513．84）pg／ml、4483．00（4130．75，4522．50）pg／ml、8170．00（8058．25，8206．75）pg／ml；12．88（12．04，13．84）pg／ml、68．51（66．88，69．77）pg／ml、335．44（331．02，340．64）pg／ml；800．57（791．18，809．60）pg／ml、1559．00（1546．00，1566．00）pg／ml、4316．50（4094．75，4389．75）pg／ml]均明显增加，差异均有统计学意义（u值均〈0．001，P值均〈0．01）；但4h、8h和24h的ID-10释放量[不处理对照组分别为1．23（1．21，1．31）pg／ml、1.56（1．31，1．82）pg／ml、5．41（4．99，5．89）pg／ml；H37Rv膜囊泡处理组分别为4．56（4．49，4．82）pg／ml、1．43（1．28，1．89）pg／ml、1．56（1．48，1．68）pg／ml]差异均无统计学意义（U值分别为6．00、17.00、7．00，P值分别为0．065、0．898和0．087）。结论本研究建立了结核分枝杆菌膜囊泡分离提取的技术流程，可以得到纯度较好、形态完整、粒径正常的膜囊泡。同时，结核分枝杆菌膜囊泡可以诱发巨噬细胞中细胞因子TNF-α、IL-6和IL-1β的释放。展开更多
大多数细胞内都包含靶向不同细胞器的各种运输囊泡,其运输机制在进化上是高度保守的。Sec1/Munc-18(SM)蛋白在膜泡运输中起着重要的调控作用,它能够与SNARE(Soluble N-ethylmaleimide-sensitive factorattachment protein receptor)蛋...大多数细胞内都包含靶向不同细胞器的各种运输囊泡,其运输机制在进化上是高度保守的。Sec1/Munc-18(SM)蛋白在膜泡运输中起着重要的调控作用,它能够与SNARE(Soluble N-ethylmaleimide-sensitive factorattachment protein receptor)蛋白结合,共同在细胞内各个膜融合发生部位发挥重要作用。SM蛋白和SNARE复合体中的Syntaxin蛋白结合,调节SNARE复合体的装配,并与SNARE协同作用促进整个膜融合过程。文章对SM蛋白在结构和功能分析方面的最新研究进展进行了概述。展开更多
基金This work was funded by the State"863"Tech Program of China under contract High No.2002AA629120the National Natural Science Foundation of China under contract No.40476060the Canadian Institute for Health Research under contract No.M0P-64465.
文摘SNARE proteins are a group of membrane-associated proteins involved in exocytosis, secretion and membrane trafficking events in eukaryotic cells. Research on SNARE protein biology has become a more attractive field in recent years, which is applied to marine biology specifically to the fish Tilapia （Oreochromis niloticus）. Plasma membrane fractions of different tissues of Tilapia, including brain, liver-pancreas, intestine, skin and muscle, were extracted, and immuno-decorated with isoform-specific antibodies to the SNARE families and associated proteins. The presence of Syntaxins - 1 A, 2 and 3, SNAP - 23 and SNAP - 25, VAMP - 2, Munc - 18 - 1 and Munc - 13 in the brain was identified, which were differentially distributed in the other organ tissues of the fish Tilapia. The distinct distribution of SNARE and associated proteins will serve as the basis for further investigation into their special secretory function in these tissues of the fish.
文摘The role of SNARE [soluble NSF (N-ethylmaleimide-sensitive factor) accessory protein receptor] protein in cellular trafficking, membrane fusion and vesicle release in synaptic nerve terminals is described. The purpose of this review is to highlight the role of SNAREs in vital inflammatory conditions in maturing dendritic cells in order to retain the capacity to present new antigens together with altered cytokine secretory functions. This role of SNAREs can be used as novel targets for therapy in inflammatory diseases. The essential mechanism of SNAREs proteins for regulation of tumour formation through multiple signals and transportation pathways is also discussed. Finally, this review summarizes the current knowledge of SNARE proteins in regulating endocytosis in cancer cells and the possible therapeutic applications related to the pathogenesis of tumor formation.
基金supported by the Ramon y Cajal programme(RYC-2007-00417,RYC-2009-05510)grants from the Spanish MINECO(SAF2013-42445R and BFU2010-21507)CIBERNED
文摘Through complex mechanisms that guide axons to the appropriate routes towards their targets, axonal growth and guidance lead to neuronal system formation. These mechanisms establish the synaptic circuitry necessary for the optimal performance of the nervous system in all organisms. Damage to these networks can be repaired by neuroregenerative processes which in turn can re-establish synapses between injured axons and postsynaptic terminals. Both axonal growth and guidance and the neuroregenerative response rely on correct axonal growth and growth cone responses to guidance cues as well as correct synapses with appropriate targets. With this in mind, parallels can be drawn between axonal regeneration and processes occurring during embryonic nervous system development. However, when studying parallels between axonal development and regeneration many questions still arise; mainly, how do axons grow and synapse with their targets and how do they repair their membranes, grow and orchestrate regenerative responses after injury. Major players in the cellular and molecular processes that lead to growth cone development and movement during embryonic development are the Soluble N-ethylamaleimide Sensitive Factor （NSF） Attachment Protein Receptor （SNARE） proteins, which have been shown to be involved in axonal growth and guidance. Their involvement in axonal growth, guidance and neuroregeneration is of foremost importance, due to their roles in vesicle and membrane trafficking events. Here, we review the recent literature on the involvement of SNARE proteins in axonal growth and guidance during embryonic development and neuroregeneration.
基金This work was supported by the National Natural Science Foundation of China (No. 30170302 39470238+3 种基金 39070323 39860249)the Climbing Project of Ministry of Science and Technology of China (No. P8505) the National Basic Research Priorities Programmeof China (No. G19999054000) and the Basic Research Program of Shanghai Municipal Commission for Science and Technology (No.O2JC14011).
文摘目的分离体外培养的结核分枝杆菌分泌的膜囊泡，检测其形态和粒径分布，初步探索结核分枝杆菌膜囊泡对巨噬细胞中细胞因子释放的作用。方法采用结核分枝杆菌实验室标准菌株H37Rv，通过7H9培养基复苏、扩大培养标准株H37Rv至对数生长期，菌体全部接种于苏通培养基中继续培养3周，离心取上清，超滤浓缩结合超速离心分离提取结核分枝杆菌H37Rv膜囊泡，通过透射电镜观察膜囊泡的大小、形态，采用纳米颗粒跟踪仪分析膜囊泡的粒径及分布。同时，设置不处理对照组、H37Rv感染组[按照感染复数（multiplicity of infection，MOI）=20：1]和H37Rv膜囊泡处理组（按照膜囊泡：细胞=100：1）处理佛波酯（50ng／ml）诱导贴壁的单核巨噬细胞（THP-1）4h，更换新鲜培养基后0h、4h、8h、24h收集细胞培养上清，采用Milliplex多细胞因子检测试剂盒检测细胞因子的释放情况，通过曼-惠特尼U（Mann-WhitneyU）检验对各时间点H37Rv膜囊泡处理组和不处理对照组之间肿瘤坏死因子α（TNF-α）、白细胞介素6（IL-6）、白细胞介素1β（IL-1β）、白细胞介素10（IL-10）释放量进行比较，以P〈0．05为差异有统计学意义。结果按照调整后的提取方法得到的提取物中可检测到H37Rv分泌的膜囊泡，平均粒径为137nm，主要分布在30～510nm之间，〈250nm的膜囊泡数量占总量的96．88％。4h、8h和24h的TNF-α、ID6和IL-1β释放量与不处理对照组[分别为348．19（333．99，360．47）pg／ml、412．38（406．67，418．79）pg／ml、324．44（316．11，331．14）pg／ml；3．01（2．81，3．02）pg／ml、5．40（5．26，5．83）pg／ml、13．22（11．80，13．77）pg／ml；118．92（113．97，122．47）pg／ml、132．33（125．87，137．62）pg／ml、169．31（167．75，172．49）pg／ml]相比，H37Rv膜囊泡处理组[分别为507．33（501．80，513．84）pg／ml、4483．00（4130．75，4522．50）pg／ml、8170．00（8058．25，8206．75）pg／ml；12．88（12．04，13．84）pg／ml、68．51（66．88，69．77）pg／ml、335．44（331．02，340．64）pg／ml；800．57（791．18，809．60）pg／ml、1559．00（1546．00，1566．00）pg／ml、4316．50（4094．75，4389．75）pg／ml]均明显增加，差异均有统计学意义（u值均〈0．001，P值均〈0．01）；但4h、8h和24h的ID-10释放量[不处理对照组分别为1．23（1．21，1．31）pg／ml、1.56（1．31，1．82）pg／ml、5．41（4．99，5．89）pg／ml；H37Rv膜囊泡处理组分别为4．56（4．49，4．82）pg／ml、1．43（1．28，1．89）pg／ml、1．56（1．48，1．68）pg／ml]差异均无统计学意义（U值分别为6．00、17.00、7．00，P值分别为0．065、0．898和0．087）。结论本研究建立了结核分枝杆菌膜囊泡分离提取的技术流程，可以得到纯度较好、形态完整、粒径正常的膜囊泡。同时，结核分枝杆菌膜囊泡可以诱发巨噬细胞中细胞因子TNF-α、IL-6和IL-1β的释放。
文摘大多数细胞内都包含靶向不同细胞器的各种运输囊泡,其运输机制在进化上是高度保守的。Sec1/Munc-18(SM)蛋白在膜泡运输中起着重要的调控作用,它能够与SNARE(Soluble N-ethylmaleimide-sensitive factorattachment protein receptor)蛋白结合,共同在细胞内各个膜融合发生部位发挥重要作用。SM蛋白和SNARE复合体中的Syntaxin蛋白结合,调节SNARE复合体的装配,并与SNARE协同作用促进整个膜融合过程。文章对SM蛋白在结构和功能分析方面的最新研究进展进行了概述。
